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Protein

Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase

Gene

yitJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

S-methyl-L-methionine + L-homocysteine = 2 L-methionine.
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarity
  • Zn2+PROSITE-ProRule annotation

Pathway: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi200 – 2001ZincPROSITE-ProRule annotation
Metal bindingi265 – 2651ZincPROSITE-ProRule annotation
Metal bindingi266 – 2661ZincPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, Metal-binding, NAD, NADP, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU11010-MONOMER.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase
Including the following 2 domains:
Homocysteine S-methyltransferase (EC:2.1.1.10)
Alternative name(s):
S-methylmethionine:homocysteine methyltransferase
5,10-methylenetetrahydrofolate reductase (EC:1.5.1.20)
Gene namesi
Name:yitJ
Ordered Locus Names:BSU11010
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU11010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 612612Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductasePRO_0000379125Add
BLAST

Proteomic databases

PaxDbiO06745.

Expressioni

Inductioni

Induced by methionine starvation.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006076.

Structurei

3D structure databases

ProteinModelPortaliO06745.
SMRiO06745. Positions 2-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 280280Hcy-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 280280Homocysteine S-methyltransferaseAdd
BLAST
Regioni295 – 6123185,10-methylenetetrahydrofolate reductaseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the methylenetetrahydrofolate reductase family.Curated
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000028409.
InParanoidiO06745.
KOiK00547.
OMAiNEVPGIQ.
OrthoDBiEOG6SNDP1.
PhylomeDBiO06745.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
3.20.20.330. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR003171. Mehydrof_redctse.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O06745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV
60 70 80 90 100
EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG
110 120 130 140 150
TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE
160 170 180 190 200
VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC
210 220 230 240 250
RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS
260 270 280 290 300
ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITEKE VKTRAKEFIS
310 320 330 340 350
VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL
360 370 380 390 400
TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL
410 420 430 440 450
DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG
460 470 480 490 500
KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ
510 520 530 540 550
LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAH
560 570 580 590 600
AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ
610
QKDEQRQNIF LH
Length:612
Mass (Da):67,928
Last modified:July 1, 1997 - v1
Checksum:iA7B6FFC2E648F800
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09476 Genomic DNA. Translation: CAA70665.1.
AL009126 Genomic DNA. Translation: CAB12941.1.
PIRiC69840.
RefSeqiNP_388982.1. NC_000964.3.
WP_003245847.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12941; CAB12941; BSU11010.
GeneIDi939796.
KEGGibsu:BSU11010.
PATRICi18973908. VBIBacSub10457_1148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09476 Genomic DNA. Translation: CAA70665.1.
AL009126 Genomic DNA. Translation: CAB12941.1.
PIRiC69840.
RefSeqiNP_388982.1. NC_000964.3.
WP_003245847.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO06745.
SMRiO06745. Positions 2-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006076.

Proteomic databases

PaxDbiO06745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12941; CAB12941; BSU11010.
GeneIDi939796.
KEGGibsu:BSU11010.
PATRICi18973908. VBIBacSub10457_1148.

Organism-specific databases

GenoListiBSU11010.

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000028409.
InParanoidiO06745.
KOiK00547.
OMAiNEVPGIQ.
OrthoDBiEOG6SNDP1.
PhylomeDBiO06745.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciBSUB:BSU11010-MONOMER.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
3.20.20.330. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR003171. Mehydrof_redctse.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees position encoding 11 membrane proteins."
    Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.
    Microbiology 143:3309-3312(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in Gram-positive bacteria."
    Grundy F.J., Henkin T.M.
    Mol. Microbiol. 30:737-749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168 / BR151.

Entry informationi

Entry nameiYITJ_BACSU
AccessioniPrimary (citable) accession number: O06745
Secondary accession number(s): Q796P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.